Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6664733 | Journal of Food Engineering | 2018 | 26 Pages |
Abstract
The functional attributes of globular proteins can be extended by controlling the nature of the aggregates they form. In this study, the effect of thermal treatment (85°C/20 min) and high pressure microfluidization (20,000 psi, 1 pass) on the physical properties of whey protein isolate solutions (5-9%; pH 2) was investigated. Heating solutions of native whey protein isolate (8 wt%) under these acidic conditions led to the formation of highly viscous solutions (η = 306 mPa s) with low turbidity (Ï = 0.04 cmâ1), which was attributed to the formation of protein fibrils (effective d = 310 nm). Microfluidization of these protein fibrils decreased their length (effective d = 97 nm) leading to a substantial reduction in solution viscosity (η = 3.8 mPa s), and a slight reduction in turbidity (Ï < 0.03 cmâ1). The impact of solution pH (2-7) on the appearance and rheology of native, heated, and heated-microfluidized whey protein isolate solutions was then examined. For all systems, highly turbid solutions (Ï > 1 cmâ1) were formed at pH values close to the isoelectric point of the whey proteins (pH 4.5) due to protein self-association caused by reduction of the electrostatic repulsion between the protein molecules. Highly viscous or gelled solutions were formed for the heated and heated-microfluidized proteins across a wide pH range, which was attributed to the presence of fibrils. The study showed that the functional attributes of whey proteins can be modulated by thermal and high-pressure homogenization treatment.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
Charmaine K.W. Koo, Cheryl Chung, Thaddao Ogren, William Mutilangi, David Julian McClements,